Structured Review

Santa Cruz Biotechnology hrp conjugated secondary antibody
Treatment with SXR activators increases expression of p53 and p53 target genes . Total RNA was isolated from A) MCF-7 cells or B) ZR75-1 cells grown in the presence of 10 μM SXR activators rifampicin, anandamide, or clotrimazole (RIF, ANA or CLO) for 72 hours and 24 hours respectively. RNA was reverse transcribed and analyzed by QRT-PCR using primers for human p53, p21, BAX and PUMA. Data are depicted as average fold induction relative to solvent control in triplicates ± S.E.M. These results were replicated in at least three independent experiments. *represents P ≤ .05, **represents P ≤ .01 and # represents P ≤ .001 (by one-way ANOVA analysis). C) SXR activation causes p53 accumulation. Cell lysates made from C) MCF-7 and D) ZR-75-1 cells treated with SXR agonists (10 μM) or solvent controls for 72 and 24 hours respectively were subjected to Western blot analysis using p53 antibody (FL-393 <t>HRP,</t> Santa <t>Cruz</t> Inc.). Equal loading was confirmed by stripping and re-probing the same blot with an anti-GAPDH antibody. Camptothecin (CAMP) 24 hour treatment was used as a positive control for p53 induction. The chemiluminescent bands were acquired by Alpha Innotech Fluorchem SP imager (Alpha Innotech Inc., CA, USA) and analyzed by spot densitometry analysis using FluorChem AlphaEase FC software (Alpha Innotech). The experiment was done in duplicates and the numbers represent the average from two independent runs. Note that the gap in ANA lane of ZR-75-1 is because of gel tearing at the time of transferring.
Hrp Conjugated Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 558 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/hrp conjugated secondary antibody/product/Santa Cruz Biotechnology
Average 92 stars, based on 558 article reviews
Price from $9.99 to $1999.99
hrp conjugated secondary antibody - by Bioz Stars, 2020-07
92/100 stars

Images

1) Product Images from "Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells"

Article Title: Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells

Journal: BMC Cancer

doi: 10.1186/1471-2407-9-3

Treatment with SXR activators increases expression of p53 and p53 target genes . Total RNA was isolated from A) MCF-7 cells or B) ZR75-1 cells grown in the presence of 10 μM SXR activators rifampicin, anandamide, or clotrimazole (RIF, ANA or CLO) for 72 hours and 24 hours respectively. RNA was reverse transcribed and analyzed by QRT-PCR using primers for human p53, p21, BAX and PUMA. Data are depicted as average fold induction relative to solvent control in triplicates ± S.E.M. These results were replicated in at least three independent experiments. *represents P ≤ .05, **represents P ≤ .01 and # represents P ≤ .001 (by one-way ANOVA analysis). C) SXR activation causes p53 accumulation. Cell lysates made from C) MCF-7 and D) ZR-75-1 cells treated with SXR agonists (10 μM) or solvent controls for 72 and 24 hours respectively were subjected to Western blot analysis using p53 antibody (FL-393 HRP, Santa Cruz Inc.). Equal loading was confirmed by stripping and re-probing the same blot with an anti-GAPDH antibody. Camptothecin (CAMP) 24 hour treatment was used as a positive control for p53 induction. The chemiluminescent bands were acquired by Alpha Innotech Fluorchem SP imager (Alpha Innotech Inc., CA, USA) and analyzed by spot densitometry analysis using FluorChem AlphaEase FC software (Alpha Innotech). The experiment was done in duplicates and the numbers represent the average from two independent runs. Note that the gap in ANA lane of ZR-75-1 is because of gel tearing at the time of transferring.
Figure Legend Snippet: Treatment with SXR activators increases expression of p53 and p53 target genes . Total RNA was isolated from A) MCF-7 cells or B) ZR75-1 cells grown in the presence of 10 μM SXR activators rifampicin, anandamide, or clotrimazole (RIF, ANA or CLO) for 72 hours and 24 hours respectively. RNA was reverse transcribed and analyzed by QRT-PCR using primers for human p53, p21, BAX and PUMA. Data are depicted as average fold induction relative to solvent control in triplicates ± S.E.M. These results were replicated in at least three independent experiments. *represents P ≤ .05, **represents P ≤ .01 and # represents P ≤ .001 (by one-way ANOVA analysis). C) SXR activation causes p53 accumulation. Cell lysates made from C) MCF-7 and D) ZR-75-1 cells treated with SXR agonists (10 μM) or solvent controls for 72 and 24 hours respectively were subjected to Western blot analysis using p53 antibody (FL-393 HRP, Santa Cruz Inc.). Equal loading was confirmed by stripping and re-probing the same blot with an anti-GAPDH antibody. Camptothecin (CAMP) 24 hour treatment was used as a positive control for p53 induction. The chemiluminescent bands were acquired by Alpha Innotech Fluorchem SP imager (Alpha Innotech Inc., CA, USA) and analyzed by spot densitometry analysis using FluorChem AlphaEase FC software (Alpha Innotech). The experiment was done in duplicates and the numbers represent the average from two independent runs. Note that the gap in ANA lane of ZR-75-1 is because of gel tearing at the time of transferring.

Techniques Used: Expressing, Isolation, Quantitative RT-PCR, Activation Assay, Western Blot, Stripping Membranes, Positive Control, Software, Transferring

2) Product Images from "Inhibition of Adipogenesis by Tempol in 3T3-L1 Cells"

Article Title: Inhibition of Adipogenesis by Tempol in 3T3-L1 Cells

Journal: Free radical biology & medicine

doi: 10.1016/j.freeradbiomed.2010.05.028

Tempol decreases the protein levels of PPAR-γ, PPAR-α , and FIAF proteins in differentiated 3T3-L1 cells A) Proteins from undifferentiated, differentiated, and Tempol-treated (2 mM)-differentiated whole cell extracts were resolved by SDS-PAGE, blotted, and probed with anti-PPAR-γ, -PPAR-α , and FIAF, and HRP-conjugated secondary antibodies. B) Levels of p21 increased upon 3T3-L1 differentiation and decreased with co-administration of 2 mM Tempol. Above each lane is the optical density value (in parenthesis) for each protein band corrected for the actin loading control using the differentiated protein level as the relative control. For FIAF, *p
Figure Legend Snippet: Tempol decreases the protein levels of PPAR-γ, PPAR-α , and FIAF proteins in differentiated 3T3-L1 cells A) Proteins from undifferentiated, differentiated, and Tempol-treated (2 mM)-differentiated whole cell extracts were resolved by SDS-PAGE, blotted, and probed with anti-PPAR-γ, -PPAR-α , and FIAF, and HRP-conjugated secondary antibodies. B) Levels of p21 increased upon 3T3-L1 differentiation and decreased with co-administration of 2 mM Tempol. Above each lane is the optical density value (in parenthesis) for each protein band corrected for the actin loading control using the differentiated protein level as the relative control. For FIAF, *p

Techniques Used: SDS Page

Related Articles

Incubation:

Article Title: Activation of the steroid and xenobiotic receptor, SXR, induces apoptosis in breast cancer cells
Article Snippet: .. The primary antibody incubation was followed by 1 hr incubation at room temperature with HRP-conjugated secondary antibody (1:10,000; Santa Cruz Biotechnology Inc., USA). .. The bands were detected using the ECL Plus Western Blotting Detection System (Amersham Bioscience, USA).

Article Title: Gene and protein patterns of potential prion-related markers in the central nervous system of clinical and preclinical infected sheep
Article Snippet: .. Next, the membranes were incubated for 1 h with HRP-conjugated secondary antibody diluted 1:3500 in blocking buffer (goat anti-mouse IgG-HRP for anti-COL1A2 and anti-MT2A or goat anti-rabbit IgG-HRP for anti-CAPN6, anti-COL3A1, anti-GALA1 and anti-MTNR1B; Santa Cruz Biotechnology). ..

Article Title: Acute Ethanol Exposure Increases the Susceptibility of the Donor Hearts to Ischemia/Reperfusion Injury after Transplantation in Rats
Article Snippet: .. After washing blots to remove excessive primary antibody binding, blots were incubated for 1 h with horseradish peroxydase conjugated secondary antibody (1∶5000, Santa Cruz Biothechnology, Heidelberg, Germany). .. The immunoreactive protein bands were developed using Enhanced Chemiluminescence system (PerkinElmer, Rodgau-Juegesheim, Germany).

other:

Article Title: Inhibition of Adipogenesis by Tempol in 3T3-L1 Cells
Article Snippet: Mouse monoclonal anti p21 and HRP-conjugated secondary antibody were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

Article Title: Cell cycle-dependent and -independent telomere shortening accompanies murine brain aging
Article Snippet: HRP-conjugated secondary antibody and the enzyme’s substrate for the chemiluminescent detection were provided within the kit.

Binding Assay:

Article Title: Acute Ethanol Exposure Increases the Susceptibility of the Donor Hearts to Ischemia/Reperfusion Injury after Transplantation in Rats
Article Snippet: .. After washing blots to remove excessive primary antibody binding, blots were incubated for 1 h with horseradish peroxydase conjugated secondary antibody (1∶5000, Santa Cruz Biothechnology, Heidelberg, Germany). .. The immunoreactive protein bands were developed using Enhanced Chemiluminescence system (PerkinElmer, Rodgau-Juegesheim, Germany).

Blocking Assay:

Article Title: HCN1 and HCN2 Proteins Are Expressed in Cochlear Hair Cells
Article Snippet: .. HRP-conjugated secondary antibodies (Santa Cruz Biotechnology) were diluted (1:6,000–1:10,000) in blocking solutions consisting of nonfat milk (1%) in PBST (plus 1% BSA for protocadherin 15 CD3) plus 2% serum corresponding to the species in which the secondary antibody was raised. .. The respective proteins were detected with Western Lightning chemiluminescence ( ).

Article Title: Gene and protein patterns of potential prion-related markers in the central nervous system of clinical and preclinical infected sheep
Article Snippet: .. Next, the membranes were incubated for 1 h with HRP-conjugated secondary antibody diluted 1:3500 in blocking buffer (goat anti-mouse IgG-HRP for anti-COL1A2 and anti-MT2A or goat anti-rabbit IgG-HRP for anti-CAPN6, anti-COL3A1, anti-GALA1 and anti-MTNR1B; Santa Cruz Biotechnology). ..

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  • 88
    Santa Cruz Biotechnology hrp conjugated goat antirabbit igg
    SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat <t>antirabbit</t> <t>IgG</t> against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P
    Hrp Conjugated Goat Antirabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology hrp conjugated anti mouse igg antibody
    Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and <t>HRP-conjugated</t> anti-mouse <t>IgG</t> antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.
    Hrp Conjugated Anti Mouse Igg Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated anti mouse igg antibody/product/Santa Cruz Biotechnology
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    85
    Santa Cruz Biotechnology goat horseradish peroxidase hrp conjugated secondary anti mouse antibody
    <t>BtaE</t> localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse <t>HRP-conjugated</t> secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.
    Goat Horseradish Peroxidase Hrp Conjugated Secondary Anti Mouse Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat horseradish peroxidase hrp conjugated secondary anti mouse antibody/product/Santa Cruz Biotechnology
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    92
    Santa Cruz Biotechnology anti pi3k p85 hrp conjugated secondary antibody
    The protein expression level of <t>PI3K</t> <t>p85.</t> Cells were treated with samples, or control for 72 h. Total protein was extracted for the analysis using Western blot. The signal of target protein in MCF-7 cells ( a , b ) and MDA-MB-231 cells ( c , d ) was detected and quantified using SuperSignal ELISA Pico Chemiluminescent Substrate. Data are presented as mean ± SD. * indicates a significant difference compared to the control ( p
    Anti Pi3k P85 Hrp Conjugated Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat antirabbit IgG against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P

    Journal: Clinical and Developmental Immunology

    Article Title: Suppressors of Cytokine Signaling 3 Expression in Eosinophils: Regulation by PGE2 and Th2 Cytokines

    doi: 10.1155/2011/917015

    Figure Lengend Snippet: SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat antirabbit IgG against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P

    Article Snippet: The secondary antibody, HRP-conjugated goat antirabbit IgG (Santa Cruz Biotechnology, Inc.), was diluted 1 : 1000.

    Techniques: Expressing, Immunohistochemistry, Immunofluorescence, Western Blot, Incubation, Microscopy, Purification, Recombinant, Positive Control, Negative Control

    Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and HRP-conjugated anti-mouse IgG antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.

    Journal: Virology Journal

    Article Title: Cloning and expression of N22 region of Torque Teno virus (TTV) genome and use of peptide in developing immunoassay for TTV antibodies

    doi: 10.1186/1743-422X-11-96

    Figure Lengend Snippet: Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and HRP-conjugated anti-mouse IgG antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.

    Article Snippet: For immunodetection of the His fusion proteins, the primary antibody used was His probe (H-3) mouse monoclonal IgG (1 : 500; Santa Cruz Biotechnology, USA) and the secondary antibody was HRP-conjugated anti-mouse IgG antibody (1 : 2000; Santa Cruz Biotechnology, USA).

    Techniques: Expressing, Recombinant, Staining, SDS Page, Incubation, Marker, Western Blot, Blocking Assay

    BtaE localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse HRP-conjugated secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.

    Journal: Infection and Immunity

    Article Title: BtaE, an Adhesin That Belongs to the Trimeric Autotransporter Family, Is Required for Full Virulence and Defines a Specific Adhesive Pole of Brucella suis

    doi: 10.1128/IAI.01241-12

    Figure Lengend Snippet: BtaE localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse HRP-conjugated secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.

    Article Snippet: Blots were probed with polyclonal mouse anti-BtaE serum (1:8,000) and a goat horseradish peroxidase (HRP)-conjugated secondary anti-mouse antibody (1:30,000; Santa Cruz) and then revealed using ECL Plus (Amersham).

    Techniques: Western Blot, SDS Page, Incubation, Immunofluorescence, Labeling, Microscopy

    The protein expression level of PI3K p85. Cells were treated with samples, or control for 72 h. Total protein was extracted for the analysis using Western blot. The signal of target protein in MCF-7 cells ( a , b ) and MDA-MB-231 cells ( c , d ) was detected and quantified using SuperSignal ELISA Pico Chemiluminescent Substrate. Data are presented as mean ± SD. * indicates a significant difference compared to the control ( p

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Synergistic Effect of Bioactive Anticarcinogens from Soybean on Anti-Proliferative Activity in MDA-MB-231 and MCF-7 Human Breast Cancer Cells In Vitro

    doi: 10.3390/molecules23071557

    Figure Lengend Snippet: The protein expression level of PI3K p85. Cells were treated with samples, or control for 72 h. Total protein was extracted for the analysis using Western blot. The signal of target protein in MCF-7 cells ( a , b ) and MDA-MB-231 cells ( c , d ) was detected and quantified using SuperSignal ELISA Pico Chemiluminescent Substrate. Data are presented as mean ± SD. * indicates a significant difference compared to the control ( p

    Article Snippet: Anti-PI3K p85 HRP-conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) were used.

    Techniques: Expressing, Western Blot, Multiple Displacement Amplification, Enzyme-linked Immunosorbent Assay